ID A0A0A1DWY6_STRSL Unreviewed; 230 AA.
AC A0A0A1DWY6;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 58.
DE RecName: Full=2,3-bisphosphoglycerate-dependent phosphoglycerate mutase {ECO:0000256|HAMAP-Rule:MF_01039};
DE Short=BPG-dependent PGAM {ECO:0000256|HAMAP-Rule:MF_01039};
DE Short=PGAM {ECO:0000256|HAMAP-Rule:MF_01039};
DE Short=Phosphoglyceromutase {ECO:0000256|HAMAP-Rule:MF_01039};
DE Short=dPGM {ECO:0000256|HAMAP-Rule:MF_01039};
DE EC=5.4.2.11 {ECO:0000256|HAMAP-Rule:MF_01039};
GN Name=gpmA_6 {ECO:0000313|EMBL:VED88508.1};
GN Synonyms=gpmA {ECO:0000256|HAMAP-Rule:MF_01039};
GN ORFNames=CQA85_01965 {ECO:0000313|EMBL:PCR83421.1}, CYK22_02795
GN {ECO:0000313|EMBL:PKZ95250.1}, DWV94_04315
GN {ECO:0000313|EMBL:RGW04537.1}, DWY30_03530
GN {ECO:0000313|EMBL:RGR62502.1}, FHI56_06475
GN {ECO:0000313|EMBL:QEM32554.1}, FOC73_09605
GN {ECO:0000313|EMBL:QKH71379.1}, HRE60_04075
GN {ECO:0000313|EMBL:QMI50861.1}, NCTC8618_03366
GN {ECO:0000313|EMBL:VED88508.1};
OS Streptococcus salivarius.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1304 {ECO:0000313|EMBL:VED88508.1, ECO:0000313|Proteomes:UP000267969};
RN [1] {ECO:0000313|EMBL:PCR83421.1, ECO:0000313|Proteomes:UP000218512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT 14-1770-C1 {ECO:0000313|EMBL:PCR83421.1,
RC ECO:0000313|Proteomes:UP000218512};
RA Ehlers B., Leendertz F.H.;
RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PKZ95250.1, ECO:0000313|Proteomes:UP000234759}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UMB0051 {ECO:0000313|EMBL:PKZ95250.1,
RC ECO:0000313|Proteomes:UP000234759};
RA Thomas-White K., Wolfe A.J.;
RT "Phylogenetic diversity of female urinary microbiome.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000284069, ECO:0000313|Proteomes:UP000285408}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF13-49B {ECO:0000313|EMBL:RGW04537.1,
RC ECO:0000313|Proteomes:UP000284069}, and AF24-6AC
RC {ECO:0000313|EMBL:RGR62502.1, ECO:0000313|Proteomes:UP000285408};
RA Zou Y., Xue W., Luo G.;
RT "A genome reference for cultivated species of the human gut microbiota.";
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:VED88508.1, ECO:0000313|Proteomes:UP000267969}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC8618 {ECO:0000313|EMBL:VED88508.1,
RC ECO:0000313|Proteomes:UP000267969};
RG Pathogen Informatics;
RL Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000313|EMBL:QEM32554.1, ECO:0000313|Proteomes:UP000322622}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LAB813 {ECO:0000313|EMBL:QEM32554.1,
RC ECO:0000313|Proteomes:UP000322622};
RA Levesque C.M., Gong S.-G., Dufour D., Barbour A.;
RT "Complete genome sequence of Streptococcus salivarius LAB813.";
RL Submitted (JUN-2019) to the EMBL/GenBank/DDBJ databases.
RN [6] {ECO:0000313|EMBL:QMI50861.1, ECO:0000313|Proteomes:UP000516705}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DB-B5 {ECO:0000313|EMBL:QMI50861.1,
RC ECO:0000313|Proteomes:UP000516705};
RX PubMed=33004456;
RA Fields F.R., Li X., Navarre W.W., Naito M.;
RT "Complete Genome Sequence of Streptococcus salivarius DB-B5, a Novel
RT Probiotic Candidate Isolated from the Supragingival Plaque of a Healthy
RT Female Subject.";
RL Microbiol. Resour. Announc. 9:e00916-e00920(2020).
RN [7] {ECO:0000313|EMBL:QKH71379.1, ECO:0000313|Proteomes:UP000501198}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FDAARGOS_771 {ECO:0000313|EMBL:QKH71379.1,
RC ECO:0000313|Proteomes:UP000501198};
RA Pederson C., Tallon L., Sadzewicz L., Zhao X., Vavikolanu K., Mehta A.,
RA Aluvathingal J., Nadendla S., Myers T., Yan Y., Sichtig H.;
RT "FDA dAtabase for Regulatory Grade micrObial Sequences (FDA-ARGOS):
RT Supporting development and validation of Infectious Disease Dx tests.";
RL Submitted (MAY-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the interconversion of 2-phosphoglycerate and 3-
CC phosphoglycerate. {ECO:0000256|HAMAP-Rule:MF_01039}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate;
CC Xref=Rhea:RHEA:15901, ChEBI:CHEBI:58272, ChEBI:CHEBI:58289;
CC EC=5.4.2.11; Evidence={ECO:0000256|HAMAP-Rule:MF_01039};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 3/5. {ECO:0000256|HAMAP-
CC Rule:MF_01039}.
CC -!- SIMILARITY: Belongs to the phosphoglycerate mutase family. BPG-
CC dependent PGAM subfamily. {ECO:0000256|HAMAP-Rule:MF_01039}.
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DR EMBL; NXMB01000002; PCR83421.1; -; Genomic_DNA.
DR EMBL; PKIA01000003; PKZ95250.1; -; Genomic_DNA.
DR EMBL; CP040804; QEM32554.1; -; Genomic_DNA.
DR EMBL; CP053998; QKH71379.1; -; Genomic_DNA.
DR EMBL; CP054153; QMI50861.1; -; Genomic_DNA.
DR EMBL; QRUM01000002; RGR62502.1; -; Genomic_DNA.
DR EMBL; QRZT01000006; RGW04537.1; -; Genomic_DNA.
DR EMBL; LR134274; VED88508.1; -; Genomic_DNA.
DR RefSeq; WP_002884137.1; NZ_WMYK01000007.1.
DR AlphaFoldDB; A0A0A1DWY6; -.
DR GeneID; 77297986; -.
DR KEGG; ssah:HSISS4_00783; -.
DR KEGG; strs:SSAL8618_04680; -.
DR UniPathway; UPA00109; UER00186.
DR Proteomes; UP000218512; Unassembled WGS sequence.
DR Proteomes; UP000234759; Unassembled WGS sequence.
DR Proteomes; UP000267969; Chromosome 1.
DR Proteomes; UP000284069; Unassembled WGS sequence.
DR Proteomes; UP000285408; Unassembled WGS sequence.
DR Proteomes; UP000322622; Chromosome.
DR Proteomes; UP000501198; Chromosome.
DR Proteomes; UP000516705; Chromosome.
DR GO; GO:0046538; F:2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniRule.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule.
DR CDD; cd07067; HP_PGM_like; 1.
DR Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR HAMAP; MF_01039; PGAM_GpmA; 1.
DR InterPro; IPR013078; His_Pase_superF_clade-1.
DR InterPro; IPR029033; His_PPase_superfam.
DR InterPro; IPR005952; Phosphogly_mut1.
DR NCBIfam; TIGR01258; pgm_1; 1.
DR PANTHER; PTHR11931; PHOSPHOGLYCERATE MUTASE; 1.
DR PANTHER; PTHR11931:SF0; PHOSPHOGLYCERATE MUTASE; 1.
DR Pfam; PF00300; His_Phos_1; 1.
DR PIRSF; PIRSF000709; 6PFK_2-Ptase; 2.
DR SMART; SM00855; PGAM; 1.
DR SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
PE 3: Inferred from homology;
KW Gluconeogenesis {ECO:0000256|HAMAP-Rule:MF_01039};
KW Glycolysis {ECO:0000256|HAMAP-Rule:MF_01039};
KW Isomerase {ECO:0000256|HAMAP-Rule:MF_01039, ECO:0000313|EMBL:VED88508.1}.
FT ACT_SITE 9
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01039,
FT ECO:0000256|PIRSR:PIRSR613078-1"
FT ACT_SITE 87
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01039,
FT ECO:0000256|PIRSR:PIRSR613078-1"
FT BINDING 8..15
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01039,
FT ECO:0000256|PIRSR:PIRSR613078-2"
FT BINDING 21..22
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01039,
FT ECO:0000256|PIRSR:PIRSR613078-2"
FT BINDING 60
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01039,
FT ECO:0000256|PIRSR:PIRSR613078-2"
FT BINDING 87..90
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01039,
FT ECO:0000256|PIRSR:PIRSR613078-2"
FT BINDING 98
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01039,
FT ECO:0000256|PIRSR:PIRSR613078-2"
FT BINDING 114..115
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01039,
FT ECO:0000256|PIRSR:PIRSR613078-2"
FT BINDING 183..184
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01039,
FT ECO:0000256|PIRSR:PIRSR613078-2"
FT SITE 182
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01039,
FT ECO:0000256|PIRSR:PIRSR613078-3"
SQ SEQUENCE 230 AA; 26106 MW; 88BAD791AFE52603 CRC64;
MVKLVFARHG ESEWNKANLF TGWADVDLSE KGTQQAIDAG KLIKEAGIEF DQAYTSVLKR
AIKTTNLALE ASDQLWVPVE KSWRLNERHY GGLTGKNKAE AAEQFGDEQV HIWRRSYDVL
PPAMDRDDEH SAHTDRRYAS LDDSVIPDAE NLKVTLERAL PFWEDKIAPA LKDGKNVFVG
AHGNSIRALV KHIKQLSDDE IMDVEIPNFP PLVFEFDEKL NVVNEYYLGK
//